Research workbench
Crystal structure of neisseria gonorrhoeae serine acetyltransferase (cyse) in complex with serine
Analyse Crystal structure of neisseria gonorrhoeae serine acetyltransferase (cyse) in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RA4
- Type
- protein
- Length
- 726 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serine acetyltransferase
- EC
- 2.3.1.30
- UniProt
- Q5F6X0
- Ligands
- SER
- Pockets
- 12 · best druggability 0.74
Structure
x-ray diffraction · 3 distinct chains · 44% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine acetyltransferase (EC 2.3.1.30) | protein | 243 | 45% helix, 14% strand | Q5F6X0 |
| B | Serine acetyltransferase (EC 2.3.1.30) | protein | 241 | 44% helix, 15% strand | Q5F6X0 |
| C | Serine acetyltransferase (EC 2.3.1.30) | protein | 242 | 42% helix, 14% strand | Q5F6X0 |
Ligands and binding sites
- SER · Serine · ligand · 2 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 689 | 0.74 | 0.80 | 60 | empty |
| 2 | 542 | 0.73 | 0.82 | 77 | empty |
| 3 | 386 | 0.72 | 0.83 | 56 | SER |
| 4 | 61 | 0.71 | 0.97 | 18 | empty |
| 5 | 52 | 0.70 | 0.98 | 19 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1166 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 1070 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 1039 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 7RA4 · Crystal structure of Neisseria gonorrhoeae serine acetyltransferase (CysE) in complex… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q5F6X0
- Elsewhere: RCSB PDB 7RA4 · PDBe 7RA4 · UniProt Q5F6X0
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